2qcs

A complex structure between the Catalytic and Regulatory subunit of Protein Kinase A that represents the inhibited state

Method: X-RAY DIFFRACTION Dmax: 98.4 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

cAMP-dependent protein kinase, alpha-catalytic subunit

Mus musculus

UniProt P05132

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–351 Fragment:CATALYTIC SUBUNIT Non-standard monomer:Yes (specific site not provided by mmCIF) cAMP-dependent protein kinase type I-alpha regulatory subunit × 1 (P00514) MN MANGANESE (II) ION × 2 SO4 SULFATE ION × 6 ACT ACETATE ION × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;298 K;2.0M(NH4)2SO4, 0.1M Citrate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.20 Å R-free 0.225

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

84 other PDB entries and 99 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAPCA_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–350; UniProt 2–351

cAMP-dependent protein kinase type I-alpha regulatory subunit

Bos taurus

UniProt P00514

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 91–380 Fragment:REGULATORY SUBUNIT Mutation:R333K cAMP-dependent protein kinase, alpha-catalytic subunit × 1 (P05132) MN MANGANESE (II) ION × 2 SO4 SULFATE ION × 6 ACT ACETATE ION × 1 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;298 K;2.0M(NH4)2SO4, 0.1M Citrate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.20 Å R-free 0.225

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

25 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KAP0_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–290; UniProt 91–380

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2qcs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2qcs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2qcs
Deposition date deposition_date2007-06-19
Structure title titleA complex structure between the Catalytic and Regulatory subunit of Protein Kinase A that represents the inhibited state
Keywords keywords;cyclic adenosine monophosphate, cAMP-dependent protein kinase, PKA holoenzyme, cyclic nucleotide binding domain, protein-protein interaction, conformational change, PROTEIN BINDING, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX ;; TRANSFERASE/TRANSFERASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier28.69
Radius of gyration Rg (electron density) rg_electron27.63
Forward intensity I(0) i087620700.00
Molecular weight molecular_weight73352.0 kDa
Excluded volume excluded_volume91707 ų
Envelope volume envelope_volume112800 ų
Hydration-shell volume shell_volume34210 ų
Envelope diameter envelope_diameter102.1
Shell Rg shell_rg34.61
Envelope Rg envelope_rg28.04
Shape Rg shape_rg27.61
Total Rg total_rg28.36
Total atoms total_atoms5154
Residues n_residues626
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax98.4
Rg (real space) rg_real28.68
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real8.7620e+07
I(0) uncertainty (real space) i0_real_error1.4340e+06
Rg (reciprocal space) rg_reciprocal28.69
I(0) (reciprocal space) i0_reciprocal87620000.0000
Solution quality estimate total_estimate0.8767
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.2
Skewness Skewness skewness0.351
Kurtosis Kurtosis kurtosis-0.233
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18160000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.818; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2qcsa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (4 domains)

Domain ID domain_id2qcsA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id2qcsA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id2qcsB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls
Domain ID domain_id2qcsB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls

8. Citations (1)

9. Files and Curves (10)